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Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle

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  • Holger Stark
  • Prakash Dube
  • Reinhard Lührmann
  • Berthold Kastner

Abstract

In eukaryotic cells, freshly synthesized messenger RNA (pre-mRNA) contains stretches of non-coding RNA that must be excised before the RNA can be translated into protein. Their removal is catalysed by the spliceosome, a large complex formed when a number of small nuclear ribonucleoprotein particles (snRNPs) bind sequentially to the pre-mRNA. The first snRNP to bind is called U1; other snRNPs (U2, U4/U6 and U5) follow1. Here we describe the three-dimensional structure of human U1 snRNP, determined by single-particle electron cryomicroscopy at 10 Å resolution. The reconstruction reveals a doughnut-shaped central element that accommodates the seven Sm proteins common to all snRNPs, supporting a proposed model of circular Sm protein arrangement2. By taking earlier biochemical results into account, we were able to assign the remaining density of the map to the other known components of U1 snRNP, deriving a structural model that describes the three-dimensional arrangement of proteins and RNA in U1 snRNP.

Suggested Citation

  • Holger Stark & Prakash Dube & Reinhard Lührmann & Berthold Kastner, 2001. "Arrangement of RNA and proteins in the spliceosomal U1 small nuclear ribonucleoprotein particle," Nature, Nature, vol. 409(6819), pages 539-542, January.
    • Handle: RePEc:nat:nature:v:409:y:2001:i:6819:d:10.1038_35054102
    DOI: 10.1038/35054102
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    1. Josef Pánek & Adriana Roithová & Nenad Radivojević & Michal Sýkora & Archana Bairavasundaram Prusty & Nicholas Huston & Han Wan & Anna Marie Pyle & Utz Fischer & David Staněk, 2023. "The SMN complex drives structural changes in human snRNAs to enable snRNP assembly," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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